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Discovery, structural characterization, and functional insights into a novel apiosidase from the GH140 family, isolated from a lignocellulolytic-enriched mangrove microbial community

Lookup NU author(s): Dr David BolamORCiD

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Abstract

© 2024, The Author(s), under exclusive licence to Springer Nature B.V. Objectives: Apiosidases are enzymes that cleave the glycosidic bond between the monosaccharides linked to apiose, a branched chain furanose found in the cell walls of vascular plants and aquatic monocots. There is biotechnological interest in this enzyme group because apiose is the flavor-active compound of grapes, fruit juice, and wine, and the monosaccharide is found to be a plant secondary metabolite with pharmaceutical properties. However, functional and structural studies of this enzyme family are scarce. Recently, a glycoside hydrolase family member GH140 was isolated from Bacteroides thetaiotaomicron and identified as an endo-apiosidase. Results: The structural characterization and functional identification of a second GH140 family enzyme, termed MmApi, discovered through mangrove soil metagenomic approach, are described. Among the various substrates tested, MmApi exhibited activity on an apiose-containing oligosaccharide derived from the pectic polysaccharide rhamnogalacturonan-II. While the crystallographic model of MmApi was similar to the endo-apiosidase from Bacteroides thetaiotaomicron, differences in the shape of the binding sites indicated that MmApi could cleave apioses within oligosaccharides of different compositions. Conclusion: This enzyme represents a novel tool for researchers interested in studying the physiology and structure of plant cell walls and developing biocatalytic strategies for drug and flavor production.

Publication metadata

Author(s): Liberato MV, Paixao DAA, Tomazetto G, Ndeh D, Bolam DN, Squina FM

Publication type: Article

Publication status: Published

Journal: Biotechnology Letters

Year: 2024

Volume: 46

Pages: 201-211

Print publication date: 01/04/2024

Online publication date: 27/01/2024

Acceptance date: 14/12/2023

ISSN (print): 0141-5492

ISSN (electronic): 1573-6776

Publisher: Springer Nature

URL: https://doi.org/10.1007/s10529-023-03460-1

DOI: 10.1007/s10529-023-03460-1

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